A D-galactose-binding lectin purified from coronate moon turban, Turbo (Lunella) coreensis, with a unique amino acid sequence and the ability to recognize lacto-series glycosphingolipids

被引：17

作者：

Fujii, Yuki ^{[1
]}

Kawsar, Sarkar M. A. ^{[1
]}

Matsumoto, Ryo ^{[1
]}

Yasumitsu, Hidetaro ^{[1
]}

Ishizaki, Naoto ^{[2
]}

Dogasaki, Chikaku ^{[2
]}

Hosono, Masahiro ^{[3
]}

Nitta, Kazuo ^{[3
]}

Hamako, Jiharu ^{[4
]}

Taei, Matsui ^{[4
]}

Ozeki, Yasuhiro ^{[1
]}

机构：

[1] Yokohama City Univ, Grad Sch NanoBiosci, Dept Genome Syst Sci, Lab Glycobiol & Marine Biochem,Kanazawa Ku, Yokohama, Kanagawa 2360027, Japan

[2] Azabu Univ, Fac Environm Hlth Sci, Dept Food & Hyg, Sagamihara, Kanagawa 2298501, Japan

[3] Tohoku Pharmaceut Univ, Inst Mol Biomembrane & Glycobiol, Div Cell Recognit Study, Aoba Ku, Sendai, Miyagi 9818558, Japan

[4] Fujita Hlth Univ, Sch Hlth Sci, Dept Biol, Aichi 4701192, Japan

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 2011年 / 158卷 / 01期

基金：

日本学术振兴会;

关键词：

Amino acid sequence; Bacterial aggregation; Frontal affinity chromatography; D-Galactose-binding lectin; Coronate moon turban shell (Turbo (Lunella) coreensis); C-TYPE LECTIN; MOLECULAR CHARACTERIZATION; PURIFICATION; IDENTIFICATION; SPECIFICITY; EXPRESSION; GALECTIN; PROTEINS; PROFILE; TRYPSIN;

D O I：

10.1016/j.cbpb.2010.09.002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A divalent, cation-independent D-galactose-binding lectin was purified from coronate moon turban Turbo (Lunen) coreensis. This lectin recognizes D-galactose and is a 38-kDa dimeric protein consisting disulphide-bonded 22-kDa polypeptides under non-reducing and reducing conditions of sodium dodecyl sulphate-polyacrylamide gel electrophoresis, respectively. Haemagglutination activity was inhibited by D-galactose, N-acetyl D-galactosamine, melibiose, lactose, porcine stomach mucin, asialofetuin and bovine submaxillary mucin. The lectin has tolerance for pH 5-11 and temperature until 50 degrees C for 1 h. The lectin strongly aggregated Gram-negative bacteria, such as Vibrio parahaemolyticus and Salmonella 07, but weakly Gram-positive strain as Staphylococcus aureus and Bacillus subtilis. The glycan-binding profile of this lectin was evaluated using frontal affinity chromatography technology and the lectin appeared to recognize oligosaccharides such as lacto-series glycosphingolipids contained in blood type A and H substances in addition to complex-type N-linked glycoproteins. Partial primary structures of 139 amino acid residues of this lectin were determined from N-terminus polypeptides and 8 peptides derived by cleavage with lysyl-endopeptidase. The primary structure was slightly similar to other known sequences of lectin: however, a repeating motif has been included. (C) 2010 Elsevier Inc. All rights reserved.

引用

页码：30 / 37

页数：8